Improvement of Fermentation Conditions for the Production of X-Prolyl-Dipeptidyl Aminopeptidase from Lactococcus Lactis

Pérez-Guzmán, Alfredo E.; Victoria, Teresa Cruz y; Cruz‐Camarillo, Ramón; Hernández‐Sánchez, Humberto

doi:10.1023/b:wibi.0000033066.86658.34

Cited by 12 publications

(5 citation statements)

References 23 publications

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“…Enzymatic activity was determined with Gly-Pro-pnitroanilide as a substrate as described previously (Pérez-Guzmán et al 2004). Western blot samples (1.5 mL) were centrifuged at 16,000g for 2.5 min.…”

Section: Monitoring Hdppiv Expression and Baculovirus Replication Witmentioning

confidence: 99%

“…The enzyme is also known as an important signaling molecule CD26 on T and B lymphocytes and it is expressed in a variety of cell types, microbial (Demuth and Heins 1995;Cunningham and O'Connor 1997;Pérez-Guzmán et al 2004), insect cells and nearly all mammalian tissues. hDPPIV regulates various physiological processes including immune system, endocrine functions, central nervous system, gastrointestinal system, inflammation, rheumatoid arthritis and cell adhesion.…”

Section: Introductionmentioning

confidence: 99%

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Monitoring of the effects of transfection with baculovirus on Sf9 cell line and expression of human dipeptidyl peptidase IV

et al. 2013

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Human dipeptidylpeptidase IV (hDPPIV) is an enzyme that is in hydrolase class and has various roles in different parts of human body. Its deficiency may cause some disorders in the gastrointestinal, neurologic, endocrinological and immunological systems of humans. In the present study, hDPPIV enzyme was expressed on Spodoptera frugiperda (Sf9) cell lines as a host cell, and the expression of hDPPIV was obtained by a baculoviral expression system. The enzyme production, optimum multiplicity of infection, optimum transfection time, infected and uninfected cell size and cell behavior during transfection were also determined. For maximum hDPPIV (269 mU mL -1 ) enzyme, optimum multiplicity of infection (MOI) and time were 0.1 and 72 h, respectively. The size of infected cells increased significantly (P \ 0.001) after 24 h post infection. The results indicated that Sf9 cell line was applicable to the large scale for hDPPIV expression by using optimized parameters (infection time and MOI) because of its high productivity (4.03 mU m L -1 h -1 ).

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Section: Monitoring Hdppiv Expression and Baculovirus Replication Witmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Monitoring of the effects of transfection with baculovirus on Sf9 cell line and expression of human dipeptidyl peptidase IV

et al. 2013

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“…N2 (pH 8.5 and 50 C) (Lee et al, 1998), Streptomyces LAP (8e8.5 and 50e65 C) (Nagy, Nampoothiri, Pandey, Rahulan, & Szakacs, 2008), and B. thuringiensis israelensis LAP (pH 10 and 65 C) (Cahan et al, 2007). The isolated LAP also differs in optimum pH from a 110-kDa L. lactis peptidase (pH 8.5) (Baankreis & Exterkate, 1991), and in optimum temperature (45 C) from L. lactis X-prolyl aminopeptidase (Pérez-Guzmán, Cruz, Victoria, Cruz-Camarillo, & Hernández-Sánchez, 2004).…”

Section: Characterisation Of Isolated Aminopeptidasementioning

confidence: 94%

Purification and characterisation of a leucine aminopeptidase from Lactococcus lactis subsp. lactis cultured in skim milk

2011

International Dairy Journal

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“…cremoris NRRL 634 was obtained from the Microbial Genomics and Bioprocessing Research Unit, of the United States Department of Agriculture. The cultures were grown at 30°C, in a modified M-17 broth which contained the following ingredients added to 1 l of distilled water: polypeptone 5 g; soy peptone 5 g; meat extract 5 g; yeast extract 3.5 g; glucose 5 g; ascorbic acid 0.5 g; sodium b-glycerophosphate 19 g and 1 ml of 1 M magnesium sulphate (Terzhaghi & Sandine 1975;Pe´rez-Guzma´n et al 2004). The medium was adjusted to pH 6.6 and autoclaved for 15 min at 121°C.…”

Section: Growth Conditionsmentioning

confidence: 99%

“…lactis, and in Lactococcus lactis subsp. cremoris (Pe´rez-Guzma´n et al 2004), showing the ubiquity of the enzyme.…”

Section: Introductionmentioning

confidence: 98%

Purification and characterization of x-prolyl-dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris NRRL 634

Pérez-Guzmán

Victoria

Cruz‐Camarillo³

et al. 2006

World J Microbiol Biotechnol

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An X-prolyl-dipeptidylaminopep tidase (Pep-XP) was purified from the crude intracellular extract of Lactococcus lactis subsp. cremoris NRRL 634 by ion exchange and gel filtration chromatographies. The enzyme was purified 80-fold with a recovery of 6%, and appeared as a single band with a molecular weight of about 80 kDa on polyacrylamide gel electrophoresis with sodium dodecyl sulphate (SDS-PAGE). The peptidase showed its maximal activity on arginyl-proline-p-nitroanilide at pH 7.0 and at a temperature of 45°C, although there was a good activity of Pep-XP in the pH range of 5.5-7.0 and temperatures between 40 and 50°C. The Michaelis constant (K m ) and the maximum reaction velocity (V max ) values were 0.92 mM and 7.9 U/mg protein min, respectively. The activity of Pep-XP was completely inhibited by phenylmethanesulphonyl fluoride, an inhibitor of serine peptidases, and metal chelators had little effect on enzyme activity. The purified enzyme hydrolyzed synthetic substrates whose structure is X-Pro-Y like Lys-Pro-pNA, but did not hydrolyse Pro-pNA or azocasein, showing that the enzyme did not have aminopeptidase or endopeptidase activities.

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Improvement of Fermentation Conditions for the Production of X-Prolyl-Dipeptidyl Aminopeptidase from Lactococcus Lactis

Cited by 12 publications

References 23 publications

Monitoring of the effects of transfection with baculovirus on Sf9 cell line and expression of human dipeptidyl peptidase IV

Monitoring of the effects of transfection with baculovirus on Sf9 cell line and expression of human dipeptidyl peptidase IV

Purification and characterisation of a leucine aminopeptidase from Lactococcus lactis subsp. lactis cultured in skim milk

Purification and characterization of x-prolyl-dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris NRRL 634

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